Ferran Feixas

This study investigates how functional and conformational substates change during enzyme evolution using single-molecule kinetic assays and simulations, showing coordinated shifts in substate equilibria that optimize catalytic efficiency.

The paper investigates how distal mutations in a retro-aldolase affect loop dynamics and catalytic efficiency, showing an epistatic effect when combined with active-site mutations.

The paper describes how two distinct enzymes evolved from a common ancestor through different mutational paths, leading to divergent molecular and phenotypic outcomes.